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7AAJ

Human porphobilinogen deaminase in complex with cofactor

Summary for 7AAJ
Entry DOI10.2210/pdb7aaj/pdb
Related7AAK
DescriptorPorphobilinogen deaminase, 3-[5-{[3-(2-carboxyethyl)-4-(carboxymethyl)-5-methyl-1H-pyrrol-2-yl]methyl}-4-(carboxymethyl)-1H-pyrrol-3-yl]propanoic acid, GLYCEROL, ... (4 entities in total)
Functional Keywordspbg-d, hydroxymethylbilane synthase, hmbs, porphobilinogen deaminase, heme biosynthesis, porphyria, acute intermittent porphyria, transferase
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total formula weight80171.39
Authors
Kallio, J.P.,Bustad, H.J.,Martinez, A. (deposition date: 2020-09-04, release date: 2021-02-17, Last modification date: 2024-01-31)
Primary citationBustad, H.J.,Kallio, J.P.,Laitaoja, M.,Toska, K.,Kursula, I.,Martinez, A.,Janis, J.
Characterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism.
Iscience, 24:102152-102152, 2021
Cited by
PubMed: 33665570
DOI: 10.1016/j.isci.2021.102152
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

221051

건을2024-06-12부터공개중

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